MolNFT v1 · #80846 · protein

The experimental X-ray structure of the new diheme cytochrome type C from shewanella baltica OS155 sb-dhc

3U99 · Diheme cytochrome C: “The experimental X-ray structure of the new diheme cytochrome type C from shewanella baltica OS155 sb-dhc”. X-ray diffraction, 1 ligand (HEC), 2 pockets (best druggability 0.65). MolNFT v1 #80846 on GenesisL1…

PDB: 3U99
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diheme cytochrome C
UniProt: A3CZ62
Ligands: HEC
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diheme cytochrome C	protein	123	43% helix, 7% strand	A3CZ62

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.65	0.84	32	HEC
2	138	0.60	0.83	21	HEC

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

3U99 · The experimental X-ray structure of the new diheme cytochrome type c from Shewanella… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A3CZ62
Elsewhere: RCSB PDB 3U99 · PDBe 3U99 · UniProt A3CZ62

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